1CVL

CRYSTAL STRUCTURE OF BACTERIAL LIPASE FROM CHROMOBACTERIUM VISCOSUM ATCC 6918

Experimental procedure

Source type	SYNCHROTRON
Source details	MPG/DESY, HAMBURG BEAMLINE BW6
Synchrotron site	MPG/DESY, HAMBURG
Beamline	BW6
Temperature [K]	293
Detector technology	IMAGE PLATE
Collection date	1993-11
Detector	MARRESEARCH
Spacegroup name	P 21 21 2
Unit cell lengths	41.080, 156.820, 43.610
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	8.000 - 1.600
R-factor	0.178 *
Rwork	0.178
Structure solution method	MIR
RMSD bond length	0.021
RMSD bond angle	0.044
Data reduction software	MOSFLM
Data scaling software	CCP4
Phasing software	MLPHARE
Refinement software	PROLSQ

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	1.640
High resolution limit [Å]	1.600	1.600
Rmerge	0.053	0.220 *
Total number of observations	87722 *
Number of reflections	33644
<I/σ(I)>	8.5	3.1
Completeness [%]	88.0	73.7
Redundancy	2.6	1.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, sitting drop *	6.4	292 *	PROTEIN WAS CRYSTALLIZED FROM 10-14 % PEG 4000, 10-14 % MPD, 100 MM CITRATE/PHOSPHATE BUFFER, PH 6.4

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	lipase	15 (mg/ml)
2	1	drop	Tris-HCl	5 (mM)
3	1	drop	n-octyl-beta-D-glycopyranoside	0.25 (%(w/v))
4	1	reservoir	PEG4000	14 (%(w/v))
5	1	reservoir	MPD	10-14 (%(v/v))
6	1	reservoir	citrate-phosphate	100 (mM)